File Download
  Links for fulltext
     (May Require Subscription)
Supplementary

Article: Multifaceted SlyD from Helicobacter pylori: implication in [NiFe] hydrogenase maturation

TitleMultifaceted SlyD from Helicobacter pylori: implication in [NiFe] hydrogenase maturation
Authors
KeywordsSlyD
Peptidylprolyl isomerase
NMR
Hydrogenase
Chaperone
Issue Date2012
PublisherSpringer Verlag. The Journal's web site is located at http://link.springer.de/link/service/journals/00775/index.htm
Citation
Journal of Biological Inorganic Chemistry, 2012, v. 17 n. 3, p. 331-343 How to Cite?
AbstractSlyD belongs to the FK506-binding protein (FKBP) family with both peptidylprolyl isomerase (PPIase) and chaperone activities, and is considered to be a ubiquitous cytosolic protein-folding facilitator in bacteria. It possesses a histidine- and cysteine-rich C-terminus binding to selected divalent metal ions (e.g., Ni(2+), Zn(2+)), which is important for its involvement in the maturation processes of metalloenzymes. We have determined the solution structure of C-terminus-truncated SlyD from Helicobacter pylori (HpSlyDDeltaC). HpSlyDDeltaC folds into two well-separated, orientation-independent domains: the PPIase-active FKBP domain and the chaperone-active insert-in-flap (IF) domain. The FKBP domain consists of a four-stranded antiparallel beta-sheet with an alpha-helix on one side, whereas the IF domain folds into a four-stranded antiparallel beta-sheet accompanied by a short alpha-helix. Intact H. pylori SlyD binds both Ni(2+) and Zn(2+), with dissociation constants of 2.74 and 3.79 muM respectively. Intriguingly, binding of Ni(2+) instead of Zn(2+) induces protein conformational changes around the active sites of the FKBP domain, implicating a regulatory role of nickel. The twin-arginine translocation (Tat) signal peptide from the small subunit of [NiFe] hydrogenase (HydA) binds the protein at the IF domain. Nickel binding and the recognition of the Tat signal peptide by the protein suggest that SlyD participates in [NiFe] hydrogenase maturation processes.
Persistent Identifierhttp://hdl.handle.net/10722/147123
ISSN
2015 Impact Factor: 2.495
2015 SCImago Journal Rankings: 0.882
PubMed Central ID
ISI Accession Number ID
Funding AgencyGrant Number
Research Grants Council of Hong KongHKU107C
HKU704207P
HKU703808P
HKU704909P
N_HKU75209
Croucher Foundation
University of Hong Kong
University Grants Committee of the Hong Kong Special Administrative Region, ChinaSEG_HKU02
Funding Information:

This work was supported by the Research Grants Council of Hong Kong (HKU107C, HKU704207P, HKU703808P, HKU704909P, N_HKU75209), the Croucher Foundation, and the University of Hong Kong. Electrospray ionization mass spectrometry was performed at the High Performance Tandem Mass Spectrometry Facility (HKU), partially supported by a Special Equipment Grant from the University Grants Committee of the Hong Kong Special Administrative Region, China (project code SEG_HKU02). The coordinates and chemical shifts of HpSlyD have been deposited in the Protein Data Bank (2KR7) and BioMagRes-Bank (16629).

References
Grants

 

DC FieldValueLanguage
dc.contributor.authorCheng, Ten_HK
dc.contributor.authorLi, Hen_HK
dc.contributor.authorXia, Wen_HK
dc.contributor.authorSun, Hen_HK
dc.date.accessioned2012-05-28T08:19:10Z-
dc.date.available2012-05-28T08:19:10Z-
dc.date.issued2012en_HK
dc.identifier.citationJournal of Biological Inorganic Chemistry, 2012, v. 17 n. 3, p. 331-343en_HK
dc.identifier.issn0949-8257en_HK
dc.identifier.urihttp://hdl.handle.net/10722/147123-
dc.description.abstractSlyD belongs to the FK506-binding protein (FKBP) family with both peptidylprolyl isomerase (PPIase) and chaperone activities, and is considered to be a ubiquitous cytosolic protein-folding facilitator in bacteria. It possesses a histidine- and cysteine-rich C-terminus binding to selected divalent metal ions (e.g., Ni(2+), Zn(2+)), which is important for its involvement in the maturation processes of metalloenzymes. We have determined the solution structure of C-terminus-truncated SlyD from Helicobacter pylori (HpSlyDDeltaC). HpSlyDDeltaC folds into two well-separated, orientation-independent domains: the PPIase-active FKBP domain and the chaperone-active insert-in-flap (IF) domain. The FKBP domain consists of a four-stranded antiparallel beta-sheet with an alpha-helix on one side, whereas the IF domain folds into a four-stranded antiparallel beta-sheet accompanied by a short alpha-helix. Intact H. pylori SlyD binds both Ni(2+) and Zn(2+), with dissociation constants of 2.74 and 3.79 muM respectively. Intriguingly, binding of Ni(2+) instead of Zn(2+) induces protein conformational changes around the active sites of the FKBP domain, implicating a regulatory role of nickel. The twin-arginine translocation (Tat) signal peptide from the small subunit of [NiFe] hydrogenase (HydA) binds the protein at the IF domain. Nickel binding and the recognition of the Tat signal peptide by the protein suggest that SlyD participates in [NiFe] hydrogenase maturation processes.en_HK
dc.languageengen_US
dc.publisherSpringer Verlag. The Journal's web site is located at http://link.springer.de/link/service/journals/00775/index.htmen_HK
dc.relation.ispartofJournal of Biological Inorganic Chemistryen_HK
dc.rightsCreative Commons: Attribution 3.0 Hong Kong Licenseen_US
dc.rightsThe original publication is available at www.springerlink.comen_US
dc.subjectSlyDen_HK
dc.subjectPeptidylprolyl isomeraseen_HK
dc.subjectNMRen_HK
dc.subjectHydrogenaseen_HK
dc.subjectChaperoneen_HK
dc.subject.meshHelicobacter pylori - enzymology-
dc.subject.meshHydrogenase - chemistry - genetics - metabolism-
dc.subject.meshIron - chemistry-
dc.subject.meshNickel - chemistry-
dc.subject.meshTacrolimus Binding Proteins - chemistry - genetics-
dc.titleMultifaceted SlyD from Helicobacter pylori: implication in [NiFe] hydrogenase maturationen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://www.springerlink.com/link-out/?id=2104&code=10546H3717981U76&MUD=MPen_US
dc.identifier.emailLi, H: hylichem@hku.hken_HK
dc.identifier.emailXia, W: weixia1984@hku.hk-
dc.identifier.emailSun, H: hsun@hku.hk-
dc.identifier.authoritySun, H=rp00777en_HK
dc.description.naturepublished_or_final_versionen_US
dc.identifier.doi10.1007/s00775-011-0855-yen_HK
dc.identifier.pmid22045417-
dc.identifier.pmcidPMC3292732-
dc.identifier.scopuseid_2-s2.0-84861911780en_HK
dc.identifier.hkuros205070-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-84861911780&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume17en_HK
dc.identifier.issue3en_HK
dc.identifier.spage331en_HK
dc.identifier.epage343en_HK
dc.identifier.eissn1432-1327en_US
dc.identifier.isiWOS:000301186000001-
dc.publisher.placeGermanyen_HK
dc.description.otherSpringer Open Choice, 28 May 2012en_US
dc.relation.projectHigh-Performance Tandem Mass Spectrometry Facility for Functional Proteomics and Metabolomics-
dc.identifier.scopusauthoridSun, H=7404827446en_HK
dc.identifier.scopusauthoridXia, W=40262950100en_HK
dc.identifier.scopusauthoridLi, H=37063577200en_HK
dc.identifier.scopusauthoridCheng, T=53879296100en_HK
dc.identifier.citeulike10001194-

Export via OAI-PMH Interface in XML Formats


OR


Export to Other Non-XML Formats